ID   THSA_SULAC              Reviewed;         558 AA.
AC   Q9V2T5; Q4J901;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Thermosome subunit alpha;
DE   AltName: Full=Chaperonin subunit alpha;
DE   AltName: Full=Thermophilic factor 55 alpha;
DE            Short=TF55-alpha;
DE   AltName: Full=Thermosome subunit 1;
GN   Name=thsA; OrderedLocusNames=Saci_1401;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-524.
RX   PubMed=10508614; DOI=10.1016/s0960-9822(99)80457-6;
RA   Archibald J.M., Logsdon J.M. Jr., Doolittle W.F.;
RT   "Recurrent paralogy in the evolution of archaeal chaperonins.";
RL   Curr. Biol. 9:1053-1056(1999).
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       and has a weak ATPase activity. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked eight-membered
CC       rings. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; CP000077; AAY80731.1; -; Genomic_DNA.
DR   EMBL; AF149923; AAF03364.1; -; Genomic_DNA.
DR   RefSeq; WP_011278233.1; NC_007181.1.
DR   AlphaFoldDB; Q9V2T5; -.
DR   SMR; Q9V2T5; -.
DR   STRING; 330779.Saci_1401; -.
DR   EnsemblBacteria; AAY80731; AAY80731; Saci_1401.
DR   GeneID; 3473404; -.
DR   KEGG; sai:Saci_1401; -.
DR   PATRIC; fig|330779.12.peg.1350; -.
DR   eggNOG; arCOG01257; Archaea.
DR   HOGENOM; CLU_008891_7_3_2; -.
DR   OMA; QTGSNDM; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd03343; cpn60; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   InterPro; IPR012714; Thermosome_arc.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02339; thermosome_arch; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..558
FT                   /note="Thermosome subunit alpha"
FT                   /id="PRO_0000128399"
FT   REGION          536..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        168
FT                   /note="F -> L (in Ref. 2; AAF03364)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182..185
FT                   /note="LVID -> DLIA (in Ref. 2; AAF03364)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="M -> T (in Ref. 2; AAF03364)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   558 AA;  59787 MW;  D958059B511D8182 CRC64;
     MAGPVLLFKE GTSRSSGRDA LRNNILAAVT LAEMLKSSLG PRGLDKMLID SFGDVTITND
     GATIVKEMEI QHPAAKLLVE AAKAQDAEVG DGTTSAVVLA GLLLDKAEEL LEQNVHPTII
     IDGYKKALTK ALEIIDQLSL KIDVNDLSSP TAKAQLKKIV STTMSSKFIA GGAEEIDKII
     DLVIDAITIV AEKRPDGTYN VPLDLIKIDK KKGGSIEDSI LVHGLVLDKE VVHAGMPRRV
     EKAKIAVLDA ALEVEKPEIS AKISITSPEQ IKSFLDEEAR YLKEMVDKLA SIGANVVICQ
     KGIDDVAQHF LAKKGILAVR RVKRSDIEKL EKALGARIIS SIKDATPEDL GYAELVEERR
     IGNDKMVFIE GAKNPRAVNI LLRGSNDMAL DEAERSLNDA LHSLRNVLMK PMIVAGGGAV
     ESELALRLRE YARSVGGKEQ LAIEKFAEAL EEIPMILAET AGMEPIQALM DLRARHAKGL
     VNSGIDAVNG KIADDMMKIN VIEPVRVKSQ VLKSAVEAAT AILKIDDLVA ASALKTEKGK
     KEGGEGAGAE TPGAPSLE